CA1305416C - Method of isolating ca 125 antigen - Google Patents
Method of isolating ca 125 antigenInfo
- Publication number
- CA1305416C CA1305416C CA000552637A CA552637A CA1305416C CA 1305416 C CA1305416 C CA 1305416C CA 000552637 A CA000552637 A CA 000552637A CA 552637 A CA552637 A CA 552637A CA 1305416 C CA1305416 C CA 1305416C
- Authority
- CA
- Canada
- Prior art keywords
- antigen
- species
- fraction
- sepharose
- urea
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 108010008629 CA-125 Antigen Proteins 0.000 title claims abstract description 44
- 102000007269 CA-125 Antigen Human genes 0.000 title claims abstract description 44
- 238000000034 method Methods 0.000 title claims abstract description 40
- 241000894007 species Species 0.000 claims abstract description 30
- 230000000694 effects Effects 0.000 claims description 58
- XSQUKJJJFZCRTK-UHFFFAOYSA-N urea group Chemical group NC(=O)N XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 52
- 229920002684 Sepharose Polymers 0.000 claims description 41
- 102000004169 proteins and genes Human genes 0.000 claims description 32
- 108090000623 proteins and genes Proteins 0.000 claims description 32
- 239000004202 carbamide Substances 0.000 claims description 30
- 206010033128 Ovarian cancer Diseases 0.000 claims description 27
- 150000001720 carbohydrates Chemical class 0.000 claims description 20
- 239000006228 supernatant Substances 0.000 claims description 20
- VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 claims description 18
- 239000002253 acid Substances 0.000 claims description 15
- 239000011347 resin Substances 0.000 claims description 14
- 229920005989 resin Polymers 0.000 claims description 14
- 230000003196 chaotropic effect Effects 0.000 claims description 12
- 238000001542 size-exclusion chromatography Methods 0.000 claims description 12
- 239000003795 chemical substances by application Substances 0.000 claims description 11
- 230000009257 reactivity Effects 0.000 claims description 11
- HPNMFZURTQLUMO-UHFFFAOYSA-N diethylamine Chemical compound CCNCC HPNMFZURTQLUMO-UHFFFAOYSA-N 0.000 claims description 10
- 239000000203 mixture Substances 0.000 claims description 10
- 239000002609 medium Substances 0.000 claims description 7
- 239000011800 void material Substances 0.000 claims description 7
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 claims description 6
- 238000003916 acid precipitation Methods 0.000 claims description 5
- 239000000872 buffer Substances 0.000 claims description 5
- 238000002270 exclusion chromatography Methods 0.000 claims description 4
- 230000002163 immunogen Effects 0.000 claims description 4
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 claims description 3
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 claims description 3
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 claims description 3
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 claims description 3
- OVRNDRQMDRJTHS-CBQIKETKSA-N N-Acetyl-D-Galactosamine Chemical compound CC(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-CBQIKETKSA-N 0.000 claims description 3
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 claims description 3
- MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 claims description 3
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 claims description 3
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 claims description 3
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 claims description 3
- 239000000727 fraction Substances 0.000 claims description 3
- 229930182830 galactose Natural products 0.000 claims description 3
- 229950006780 n-acetylglucosamine Drugs 0.000 claims description 3
- 238000000502 dialysis Methods 0.000 claims description 2
- LRPQMNYCTSPGCX-UHFFFAOYSA-N dimethyl pimelimidate Chemical compound COC(=N)CCCCCC(=N)OC LRPQMNYCTSPGCX-UHFFFAOYSA-N 0.000 claims description 2
- 239000001963 growth medium Substances 0.000 claims description 2
- 230000003472 neutralizing effect Effects 0.000 claims 3
- GNFTZDOKVXKIBK-UHFFFAOYSA-N 3-(2-methoxyethoxy)benzohydrazide Chemical compound COCCOC1=CC=CC(C(=O)NN)=C1 GNFTZDOKVXKIBK-UHFFFAOYSA-N 0.000 claims 1
- FGUUSXIOTUKUDN-IBGZPJMESA-N C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 Chemical compound C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 FGUUSXIOTUKUDN-IBGZPJMESA-N 0.000 claims 1
- 239000003463 adsorbent Substances 0.000 claims 1
- 239000006143 cell culture medium Substances 0.000 claims 1
- 239000013628 high molecular weight specie Substances 0.000 claims 1
- 230000003053 immunization Effects 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 125000005629 sialic acid group Chemical group 0.000 claims 1
- 102000036639 antigens Human genes 0.000 abstract description 57
- 108091007433 antigens Proteins 0.000 abstract description 57
- 239000000427 antigen Substances 0.000 abstract description 56
- 210000004027 cell Anatomy 0.000 description 25
- 238000011282 treatment Methods 0.000 description 21
- 210000002966 serum Anatomy 0.000 description 19
- 206010028980 Neoplasm Diseases 0.000 description 17
- 235000014633 carbohydrates Nutrition 0.000 description 17
- 238000003556 assay Methods 0.000 description 14
- 235000020256 human milk Nutrition 0.000 description 14
- 210000004251 human milk Anatomy 0.000 description 14
- 238000003127 radioimmunoassay Methods 0.000 description 14
- KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 description 13
- 238000000746 purification Methods 0.000 description 13
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 12
- 239000002953 phosphate buffered saline Substances 0.000 description 12
- 201000011510 cancer Diseases 0.000 description 11
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 10
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 10
- 206010061535 Ovarian neoplasm Diseases 0.000 description 10
- 108091005804 Peptidases Proteins 0.000 description 10
- 239000004365 Protease Substances 0.000 description 10
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 9
- 230000000890 antigenic effect Effects 0.000 description 9
- 230000029087 digestion Effects 0.000 description 9
- 210000001519 tissue Anatomy 0.000 description 9
- 230000029936 alkylation Effects 0.000 description 8
- 238000005804 alkylation reaction Methods 0.000 description 8
- 238000004587 chromatography analysis Methods 0.000 description 8
- 239000012228 culture supernatant Substances 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 102000003886 Glycoproteins Human genes 0.000 description 7
- 108090000288 Glycoproteins Proteins 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 238000004440 column chromatography Methods 0.000 description 7
- 238000010828 elution Methods 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 238000003119 immunoblot Methods 0.000 description 7
- 230000003647 oxidation Effects 0.000 description 7
- 238000007254 oxidation reaction Methods 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 6
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 6
- 238000001962 electrophoresis Methods 0.000 description 6
- 238000002955 isolation Methods 0.000 description 6
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 6
- 239000007790 solid phase Substances 0.000 description 6
- 229920000936 Agarose Polymers 0.000 description 5
- 102000015728 Mucins Human genes 0.000 description 5
- 108010063954 Mucins Proteins 0.000 description 5
- 239000003599 detergent Substances 0.000 description 5
- 229960004198 guanidine Drugs 0.000 description 5
- 230000035484 reaction time Effects 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 108010059712 Pronase Proteins 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 4
- 239000002131 composite material Substances 0.000 description 4
- 238000002298 density-gradient ultracentrifugation Methods 0.000 description 4
- 239000012153 distilled water Substances 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 150000002482 oligosaccharides Polymers 0.000 description 4
- QKFJKGMPGYROCL-UHFFFAOYSA-N phenyl isothiocyanate Chemical compound S=C=NC1=CC=CC=C1 QKFJKGMPGYROCL-UHFFFAOYSA-N 0.000 description 4
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- 108090000317 Chymotrypsin Proteins 0.000 description 3
- 108010010803 Gelatin Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 239000013060 biological fluid Substances 0.000 description 3
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 3
- 229960002376 chymotrypsin Drugs 0.000 description 3
- 238000005194 fractionation Methods 0.000 description 3
- 239000008273 gelatin Substances 0.000 description 3
- 229920000159 gelatin Polymers 0.000 description 3
- 235000019322 gelatine Nutrition 0.000 description 3
- 235000011852 gelatine desserts Nutrition 0.000 description 3
- 238000009169 immunotherapy Methods 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 239000012723 sample buffer Substances 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 102000005348 Neuraminidase Human genes 0.000 description 2
- 108010006232 Neuraminidase Proteins 0.000 description 2
- 239000000020 Nitrocellulose Substances 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 239000008351 acetate buffer Substances 0.000 description 2
- -1 alditol acetate Chemical class 0.000 description 2
- ROOXNKNUYICQNP-UHFFFAOYSA-N ammonium persulfate Chemical compound [NH4+].[NH4+].[O-]S(=O)(=O)OOS([O-])(=O)=O ROOXNKNUYICQNP-UHFFFAOYSA-N 0.000 description 2
- 230000002494 anti-cea effect Effects 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 229960003082 galactose Drugs 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 230000002637 immunotoxin Effects 0.000 description 2
- 239000002596 immunotoxin Substances 0.000 description 2
- 229940051026 immunotoxin Drugs 0.000 description 2
- 231100000608 immunotoxin Toxicity 0.000 description 2
- 229920001220 nitrocellulos Polymers 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 229940117953 phenylisothiocyanate Drugs 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- XOJVVFBFDXDTEG-UHFFFAOYSA-N pristane Chemical compound CC(C)CCCC(C)CCCC(C)CCCC(C)C XOJVVFBFDXDTEG-UHFFFAOYSA-N 0.000 description 2
- 210000000582 semen Anatomy 0.000 description 2
- 208000004548 serous cystadenocarcinoma Diseases 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- AWDRATDZQPNJFN-VAYUFCLWSA-N taurodeoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCS(O)(=O)=O)C)[C@@]2(C)[C@@H](O)C1 AWDRATDZQPNJFN-VAYUFCLWSA-N 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 239000003104 tissue culture media Substances 0.000 description 2
- 125000000026 trimethylsilyl group Chemical group [H]C([H])([H])[Si]([*])(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- 238000005199 ultracentrifugation Methods 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- BSFODEXXVBBYOC-UHFFFAOYSA-N 8-[4-(dimethylamino)butan-2-ylamino]quinolin-6-ol Chemical compound C1=CN=C2C(NC(CCN(C)C)C)=CC(O)=CC2=C1 BSFODEXXVBBYOC-UHFFFAOYSA-N 0.000 description 1
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- 238000011725 BALB/c mouse Methods 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 102000037716 Chondroitin-sulfate-ABC endolyases Human genes 0.000 description 1
- 108090000819 Chondroitin-sulfate-ABC endolyases Proteins 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 206010013457 Dissociation Diseases 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 102000002268 Hexosaminidases Human genes 0.000 description 1
- 108010000540 Hexosaminidases Proteins 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 1
- 208000007571 Ovarian Epithelial Carcinoma Diseases 0.000 description 1
- 208000007542 Paresis Diseases 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 1
- 241001632427 Radiola Species 0.000 description 1
- 101000916532 Rattus norvegicus Zinc finger and BTB domain-containing protein 38 Proteins 0.000 description 1
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 1
- 238000005852 acetolysis reaction Methods 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 102000012086 alpha-L-Fucosidase Human genes 0.000 description 1
- 108010061314 alpha-L-Fucosidase Proteins 0.000 description 1
- DUKURNFHYQXCJG-JEOLMMCMSA-N alpha-L-Fucp-(1->4)-[beta-D-Galp-(1->3)]-beta-D-GlcpNAc-(1->3)-beta-D-Galp-(1->4)-D-Glcp Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@H]1[C@H](O[C@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)[C@@H](NC(C)=O)[C@H](O[C@@H]2[C@H]([C@H](O[C@@H]3[C@H](OC(O)[C@H](O)[C@H]3O)CO)O[C@H](CO)[C@@H]2O)O)O[C@@H]1CO DUKURNFHYQXCJG-JEOLMMCMSA-N 0.000 description 1
- 229910001870 ammonium persulfate Inorganic materials 0.000 description 1
- 230000003698 anagen phase Effects 0.000 description 1
- 238000003149 assay kit Methods 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
- 244000309464 bull Species 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 229940077731 carbohydrate nutrients Drugs 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000011097 chromatography purification Methods 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 229940009976 deoxycholate Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 208000018459 dissociative disease Diseases 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 229930182470 glycoside Natural products 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 102000035122 glycosylated proteins Human genes 0.000 description 1
- 108091005608 glycosylated proteins Proteins 0.000 description 1
- 239000011544 gradient gel Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000011503 in vivo imaging Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- FKADDOYBRRMBPP-UHFFFAOYSA-N lacto-N-fucopentaose II Natural products OC1C(O)C(O)C(C)OC1OC1C(OC2C(C(O)C(O)C(CO)O2)O)C(NC(C)=O)C(OC2C(C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C2O)O)OC1CO FKADDOYBRRMBPP-UHFFFAOYSA-N 0.000 description 1
- 239000010410 layer Substances 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 229940041290 mannose Drugs 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000004264 monolayer culture Methods 0.000 description 1
- 229940051875 mucins Drugs 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000002611 ovarian Effects 0.000 description 1
- 208000012318 pareses Diseases 0.000 description 1
- 229920000915 polyvinyl chloride Polymers 0.000 description 1
- 239000004800 polyvinyl chloride Substances 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 229940070376 protein Drugs 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 238000004809 thin layer chromatography Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
- Y10S530/832—Milk; colostrum
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
- Y10S530/85—Reproductive organs or embryos
- Y10S530/852—Sperm
- Y10S530/853—Ovary; eggs; embryos
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Toxicology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Compounds Of Unknown Constitution (AREA)
- Magnetic Heads (AREA)
- Macromonomer-Based Addition Polymer (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US06/933,784 US5059680A (en) | 1986-11-24 | 1986-11-24 | Method of isolating ca 125 antigen |
| US933,784 | 1986-11-24 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1305416C true CA1305416C (en) | 1992-07-21 |
Family
ID=25464497
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000552637A Expired - Lifetime CA1305416C (en) | 1986-11-24 | 1987-11-24 | Method of isolating ca 125 antigen |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US5059680A (de) |
| EP (1) | EP0332651B2 (de) |
| JP (1) | JPH02501258A (de) |
| AT (1) | ATE97448T1 (de) |
| CA (1) | CA1305416C (de) |
| DE (1) | DE3788229T3 (de) |
| WO (1) | WO1988003954A1 (de) |
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE8901127D0 (sv) * | 1989-03-31 | 1989-03-31 | Aa H L Pousette | Reagenssats och dess anvaending foer att bilda (spap-anti-spap) -immunkomplex samt diagnostiskt foerfarand vid vilket spap detekteras |
| US5366866A (en) * | 1991-07-25 | 1994-11-22 | Duke University | Method of diagnosing ovarian and endometrial cancer with monoclonal antibodies OXA and OXB |
| US5976818A (en) * | 1991-12-16 | 1999-11-02 | The Board Of Trustees Of The University Of Arkansas | Monoclonal antibodies which identify the glycoprotein carrying the CA 125 epitope |
| US5800347A (en) * | 1995-11-03 | 1998-09-01 | The General Hospital Corporation | ROC method for early detection of disease |
| EP0957749A2 (de) * | 1995-09-12 | 1999-11-24 | The General Hospital Corporation | Verfahren zur früherkennung des eierstockrebs |
| US7318921B2 (en) | 1996-05-15 | 2008-01-15 | Altarex Medical Corp. | Therapeutic compositions that alter the immune response |
| US8038994B2 (en) | 1996-05-15 | 2011-10-18 | Quest Pharmatech Inc. | Combination therapy for treating disease |
| IL139700A (en) | 1998-06-15 | 2005-09-25 | Altarex Medical Corp | Immunotherapeutic composition for the treatment of prostate cancer |
| US6376654B1 (en) | 1999-08-13 | 2002-04-23 | Molecular Discoveries, Llc | Myeloma cell and ovarian cancer cell surface glycoproteins, antibodies thereto, and uses thereof |
| US7226750B1 (en) | 2000-08-08 | 2007-06-05 | Molecular Discoveries, Inc. | Ovarian cancer cell and myeloma cell surface glycoproteins, antibodies thereto, and uses thereof |
| US7229780B2 (en) | 2000-09-05 | 2007-06-12 | The Medical Research Council | Monoclonal antibody against ovarian carcinoma |
| WO2004035537A2 (en) | 2002-10-16 | 2004-04-29 | Euro-Celtique S.A. | Antibodies that bind cell-associated ca 125/o772p and methods of use thereof |
| EP2261255A1 (de) * | 2003-07-15 | 2010-12-15 | The Regents of The University of California | Verfahren zur Reinigung von Sialinsäure-spezifischen Antikörpern und Zusammensetzung, die die affinitätsgereinigten Antikörper enthält |
| WO2013151649A1 (en) | 2012-04-04 | 2013-10-10 | Sialix Inc | Glycan-interacting compounds |
| FI3218005T3 (fi) | 2014-11-12 | 2023-03-31 | Seagen Inc | Glykaanin kanssa vuorovaikutteisia yhdisteitä ja käyttömenetelmiä |
| US9879087B2 (en) | 2014-11-12 | 2018-01-30 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| CA3002097A1 (en) | 2015-11-12 | 2017-05-18 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| WO2018094143A1 (en) | 2016-11-17 | 2018-05-24 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
| WO2018160909A1 (en) | 2017-03-03 | 2018-09-07 | Siamab Therapeutics, Inc. | Glycan-interacting compounds and methods of use |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2630380A1 (de) * | 1975-07-14 | 1977-02-03 | Microlog Ltd | Verfahren zur herstellung einer vakzine |
| US4584278A (en) * | 1982-03-19 | 1986-04-22 | University Of Rochester | Antigen derived from human ovarian tumors and radioimmunoassay using the antigen |
| JPS60256284A (ja) * | 1984-06-01 | 1985-12-17 | Nippon Telegr & Teleph Corp <Ntt> | 動画像送受信方式 |
-
1986
- 1986-11-24 US US06/933,784 patent/US5059680A/en not_active Expired - Lifetime
-
1987
- 1987-11-20 EP EP87908082A patent/EP0332651B2/de not_active Expired - Lifetime
- 1987-11-20 WO PCT/US1987/003052 patent/WO1988003954A1/en not_active Ceased
- 1987-11-20 AT AT87908082T patent/ATE97448T1/de not_active IP Right Cessation
- 1987-11-20 JP JP63500323A patent/JPH02501258A/ja active Pending
- 1987-11-20 DE DE3788229T patent/DE3788229T3/de not_active Expired - Lifetime
- 1987-11-24 CA CA000552637A patent/CA1305416C/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| JPH02501258A (ja) | 1990-05-10 |
| US5059680A (en) | 1991-10-22 |
| DE3788229T2 (de) | 1994-04-21 |
| EP0332651A1 (de) | 1989-09-20 |
| WO1988003954A1 (en) | 1988-06-02 |
| ATE97448T1 (de) | 1993-12-15 |
| EP0332651B2 (de) | 1996-12-27 |
| DE3788229T3 (de) | 1997-04-10 |
| DE3788229D1 (de) | 1993-12-23 |
| EP0332651B1 (de) | 1993-11-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA1305416C (en) | Method of isolating ca 125 antigen | |
| Davis et al. | Characterization of the CA 125 antigen associated with human epithelial ovarian carcinomas | |
| Fuks et al. | Carcinoembryonic antigen (CEA): Molecular biology and clinical significance | |
| CA1183451A (en) | Method for producing a csap tryptic peptide and anti- csap antibodies | |
| Abe et al. | Structural analysis of the DF3 human breast carcinoma-associated protein | |
| Pancino et al. | Purification and characterisation of a breast-cancer-associated glycoprotein not expressed in normal breast and identified by monoclonal antibody 83D4 | |
| JPS63279784A (ja) | 新ムチンエピトープに対する単クローン性抗体を生成するハイブリドーマ | |
| Persson et al. | Purification of a native membrane-associated adenovirus tumor antigen | |
| Zhang et al. | Comparison of sialyl-Lewis a-carrying CD43 and MUC1 mucins secreted from a colon carcinoma cell line for E-selectin binding and inhibition of leukocyte adhesion | |
| US4269825A (en) | New glycoprotein and process for isolating it | |
| US4402872A (en) | Protein and process for isolating it | |
| Klug et al. | Purification and composition of a novel gastrointestinal tumor-associated glycoprotein expressing sialylated lacto-N-fucopentaose II (CA 19-9) | |
| Iacobelli et al. | Purification and characterization of a 90 kDa protein released from human tumors and tumor cell lines | |
| EP0351313A2 (de) | Glycoprotein und dessen kodierendes Gen | |
| EP0087898A1 (de) | Antikörper und Antigene zur Bestimmung und Behandlung von Krebs | |
| US4468345A (en) | Protein (PP17), a process for concentrating and isolating it and its use | |
| Katari et al. | Characterization of the shed form of the human tumor-associated glycoprotein (TAG-72) from serous effusions of patients with different types of carcinomas | |
| US4500451A (en) | New protein PP13 extracted from human placental tissues and use thereof | |
| HU208546B (en) | Process for producing human antibodies for treating non-small-cell pulmonary-carcinomes, hib ridomes producing them, and antigenes recognised by the antibodies, and diagnostical process and kit | |
| US4746731A (en) | Isolated tissue protein PP18 | |
| Seya et al. | Additional forms of human decay-accelerating factor (DAF). | |
| Shuichi et al. | Purification and characterization of IgE produced by human myeloma cell line, U266 | |
| Van Munster et al. | Evidence of immunochemical differences between free and bound secretory piece | |
| US5773215A (en) | Tumor marker protein for cancer risk assessment | |
| Pfeffer et al. | Biosynthesis of spectrin and its assembly into the cytoskeletal system of Friend erythroleukemia cells. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MKEX | Expiry |